Polymorphism in fowl serum albumin—I. Characterization of two genetic variants of fowl serum albumin and definition of peptide differences
Autor: | Melvin Fried, P.W. Chun |
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Rok vydání: | 1971 |
Předmět: |
Chemical Phenomena
Protein Conformation Physiology Fowl Peptide Carboxypeptidases Breeding Biochemistry Chromatography DEAE-Cellulose Diffusion Glycols Aspartic acid Chemical Precipitation Electrophoresis Paper Trypsin Amino Acids Alanine chemistry.chemical_classification biology Chemistry Physical Viscosity Circular Dichroism General Medicine Amino acid Sedimentation coefficient Ammonium Sulfate Chromatography Gel Electrophoresis Chromatography Paper Ultraviolet Rays Serum albumin Animals Immunoelectrophoresis Molecular Biology Crosses Genetic Serum Albumin Polymorphism Genetic Chromatography Lysine biology.organism_classification Molecular Weight Kinetics Optical Rotatory Dispersion chemistry Sephadex biology.protein Polyethylenes Peptides Chickens Ultracentrifugation Mathematics |
Zdroj: | Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 39:523-540 |
ISSN: | 0305-0491 |
DOI: | 10.1016/0305-0491(71)90197-0 |
Popis: | 1. 1. Two electrophoretically distinct serum albumin phenotypes, from highly inbred fowl, were isolated by high polymer fractionation and characterized physically and chemically. 2. 2. Each form contained alanine and aspartic acid as C-terminal and N-terminal amino acid residues respectively. There were no significant differences between the two in such physical parameters as sedimentation coefficient, diffusion coefficient, refractive index, viscosity or optical rotatory dispersion. 3. 3. The primary structures were studied by tryptic hydrolysis followed by peptide isolation by Sephadex G-10 gel filtration, two-dimensional finger-printing and paper electrophoresis. The structural difference between the two variants was identified as a lysine-neutral amino acid substitution by amino acid analyses of the isolated peptides. |
Databáze: | OpenAIRE |
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